Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
复制标题
DOI：
10.1016/s0092-8674(00)81593-7
复制
发表时间：
1998-08-21
期刊：
影响因子：
64.5
通讯作者：
Weis, WI
中科院分区：
文献类型：
--
作者：
Lenzen, CU;Steinmann, D;Weis, WI
N-乙基马来酰亚胺敏感融合蛋白 (NSF) 是许多细胞内囊泡融合反应所需的胞质 ATP 酶。 NSF 由与囊泡运输机制的其他组件相互作用的氨基末端区域组成，后面是两个同源 ATP 结合盒，分别称为 D1 和 D2，它们分别具有必需的 ATP 酶和六聚化活性。与 Mg2+-AMPPNP 结合的 D2 的晶体结构已在 1.75 埃分辨率下测定。该结构由一个核苷酸结合结构域和一个螺旋结构域组成，并且与大肠杆菌 DNA 聚合酶 III 的钳加载亚基 delta' 的前两个结构域出人意料地相似。该结构表明几个区域负责 ATP 水解与全长 NSF 结构变化的耦合。
N-ethylmaleimide-sensitive fusion protein (NSF) is a cytosolic ATPase required for many intracellular vesicle fusion reactions. NSF consists of an amino-terminal region that interacts with other components of the vesicle trafficking machinery, followed by two homologous ATP-binding cassettes, designated D1 and D2, that possess essential ATPase and hexamerization activities, respectively. The crystal structure of D2 bound to Mg2+-AMPPNP has been determined at 1.75 Angstrom resolution. The structure consists of a nucleotide-binding and a helical domain, and it is unexpectedly similar to the first two domains of the clamp-loading subunit delta' of E. coli DNA polymerase III. The structure suggests several regions responsible for coupling of ATP hydrolysis to structural changes in full-length NSF.